Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase (Q27640679)

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1 November 2019

title

Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase (English)

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4

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1 November 2019

author name string

Jinrong Min

1

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1 November 2019

Qin Feng

2

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1 November 2019

Zhizhong Li

3

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1 November 2019

Rui-Ming Xu

5

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1 November 2019

language of work or name

English

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publication date

1 March 2003

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1 November 2019

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1 November 2019

volume

112

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1 November 2019

issue

5

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1 November 2019

page(s)

711-723

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Gene silencing: trans-histone regulatory pathway in chromatin

1 November 2019

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Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold

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Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase

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Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain

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Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate

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Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association

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Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79.

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin

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Processing of X-ray diffraction data collected in oscillation mode

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A core nucleosome surface crucial for transcriptional silencing.

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Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

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Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase

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Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

686500

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12628190%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

686500

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

686500